An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation

Bonfiglio, J. J.; Leidecker, O.; Dauben, H.; Longarini, E. J.; Colby, T.; San Segundo-Acosta, P.; Perez, K. A.; Matic, I.

doi:10.1016/j.cell.2020.09.055

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An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation

MPG-Autoren

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Bonfiglio, J. J.
Matic – ADP-ribosylation in DNA Repair and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Leidecker, O.
Matic – ADP-ribosylation in DNA Repair and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Dauben, H.
Matic – ADP-ribosylation in DNA Repair and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Longarini, E. J.
Matic – ADP-ribosylation in DNA Repair and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Colby, T.
Matic – ADP-ribosylation in DNA Repair and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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San Segundo-Acosta, P.
Matic – ADP-ribosylation in DNA Repair and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Matic, I.
Matic – ADP-ribosylation in DNA Repair and Ageing, Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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https://www.ncbi.nlm.nih.gov/pubmed/33186521
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Zitation

Bonfiglio, J. J., Leidecker, O., Dauben, H., Longarini, E. J., Colby, T., San Segundo-Acosta, P., et al. (2020). An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation. Cell, 183(4), 1086-1102 e23. doi:10.1016/j.cell.2020.09.055.

Zitierlink: https://hdl.handle.net/21.11116/0000-000B-3066-C

Zusammenfassung

Strategies for installing authentic ADP-ribosylation (ADPr) at desired positions are fundamental for creating the tools needed to explore this elusive post-translational modification (PTM) in essential cellular processes. Here, we describe a phospho-guided chemoenzymatic approach based on the Ser-ADPr writer complex for rapid, scalable preparation of a panel of pure, precisely modified peptides. Integrating this methodology with phage display technology, we have developed site-specific as well as broad-specificity antibodies to mono-ADPr. These recombinant antibodies have been selected and characterized using multiple ADP-ribosylated peptides and tested by immunoblotting and immunofluorescence for their ability to detect physiological ADPr events. Mono-ADPr proteomics and poly-to-mono comparisons at the modification site level have revealed the prevalence of mono-ADPr upon DNA damage and illustrated its dependence on PARG and ARH3. These and future tools created on our versatile chemical biology-recombinant antibody platform have broad potential to elucidate ADPr signaling pathways in health and disease.